Evidence for a specific interaction of vitronectin with arginine: Effects of reducing agents on the expression of functional domains and immunoepitopes

摘要

Vitronectin (Vn) circulates in plasma primarily in the native, monomeric form, whereas platelet-associated Vn is sonforma- tionally altered and multimeric. Here, we report that denatured Vn specifically binds to L-Arg, whereas the L-Arg binding site is cryptic in the native form of Vn. In addition, combined treatment of disulfide-linked Vn multimers with L-Arg, urea, and reducing agent results in the formation of disperse oligomers with reduced expression of denaturation-sensitive epitopes.